Abstract

Acne vulgaris, one of the most common skin diseases, is a multifactorial problem caused by Propionibacterium acnes. Acne therapy has so limitations and dissatisfactions. Here we designed a synthetic construct containing the C-terminal amino acids of the sialidase and also N-terminal amino acids of the Camp factor (the two major virulence factors of P. acnes), and linked these two domains to each other by an appropriate linker. The chimeric gene was synthesized with codon optimization for a prokaryotic host. The mRNA structure of the construct gene and its stability as a protein were analyzed by bioinformatics tools and servers. Then, the immunogenicity, B-cell epitope and MHC binding properties of the chimeric protein were predicted. Our results showed that this fusion protein had separated domains and was stable with high antigencity and immunogenicity properties. We concluded that this structure can generate a potent immune response against acne vulgaris and may be considered as anacne vaccine candidate.